In the production of cheese it is necessary to coagulate the cheese-milk to be able to separate the cheese-matters e.g. casein from the whey. Products containing the proteolytic enzyme chymosin, which is a milk-coagulating enzyme isolated from the fourth stomach of calf, have for many years been used for this purpose. Shortage of calf stomachs has in the last decades resulted in intense research for other milk-coagulating enzymes. Today also bovine pepsin, porcine pepsin as well as microbial enzymes are used commercially. All these known milk-clotting enzymes are characterized by having specificity for the peptide bond between residues 105 (phenylalanine) and 106 (methionine) or a bond adjacent to that in κ-casein. This means that by employing these enzymes in cheese-making, the κ-casein is split at the junction between para-κ-casein and the macro-peptide moiety called glyco-macro-peptide (GMP) carrying the negative charges. When this occurs the macro-peptide diffuses into the whey, its stabilizing effect on the casein micelles is lost, and the casein micelles can start to aggregate once sufficient of their κ-casein has been hydrolysed. For further elaboration on the enzymatic coagulation of milk see e.g. D. G. Dalgleish in Advanced Dairy Chemistry vol 1 ed by P. F. Fox Elsevier, London, 1992.
It is an object of this invention to provide a novel cheese-making process using a different enzyme from known methods. It is also an object of the invention to provide a method having a higher cheese yield.